G-quadruplex-proximity protein labeling based on peroxidase activity

Peroxidase-proximity protein labeling was performed using a hemin-parallel G-quadruplex (G4) complex. A tyrosine labeling reaction using an N -methyl luminol derivative was accelerated in close proximity to the hemin with enhanced peroxidase activity by binding to parallel G4. The TERRA-hemin comple...

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Bibliographic Details
Published in:Chemical communications (Cambridge, England) England), 2020-10, Vol.56 (78), p.11641-11644
Main Authors: Masuzawa, Tatsuki, Sato, Shinichi, Niwa, Tatsuya, Taguchi, Hideki, Nakamura, Hiroyuki, Oyoshi, Takanori
Format: Article
Language:English
Subjects:
Base Sequence
Binding
Binding Sites
DNA-Binding Proteins - chemistry
DNA-Binding Proteins - metabolism
G-Quadruplexes
HeLa Cells
Hemin - chemistry
Hemin - metabolism
Heterogeneous Nuclear Ribonucleoprotein A1 - chemistry
Heterogeneous Nuclear Ribonucleoprotein A1 - genetics
Heterogeneous Nuclear Ribonucleoprotein A1 - metabolism
Humans
Labeling
Luminol - chemistry
Mutagenesis, Site-Directed
Peroxidase
Peroxidase - metabolism
Proteins
Proximity
Transcription Factors - chemistry
Transcription Factors - metabolism
Tyrosine
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Summary:Peroxidase-proximity protein labeling was performed using a hemin-parallel G-quadruplex (G4) complex. A tyrosine labeling reaction using an N -methyl luminol derivative was accelerated in close proximity to the hemin with enhanced peroxidase activity by binding to parallel G4. The TERRA-hemin complex activated the labeling of many RNA-binding proteins, including heterogeneous nuclear ribonucleoproteins, in a HeLa cell lysate. G-quadruplex-proximity protein labeling was performed using a hemin-parallel G-quadruplex (G4) complex. A tyrosine labeling reaction was accelerated in close proximity to the hemin with enhanced peroxidase activity by binding to parallel G4.
ISSN:1359-7345
1364-548X
DOI:10.1039/d0cc02571b